Lysine deacetylases (KDACs), more generally referred to as histone deactylases, are a class of enzymes found in bacteria, fungi, plants, and animals that catalyze the hydrolysis of acetylated lysine side chains in histone and non-histone proteins. These enzymes are implicated in a number of biological processes such as cell differentiation, proliferation, senescence, and apoptosis. Eighteen KDACs have been identified in the human genome. Eleven human KDACs are zinc-dependent enzymes; an additional seven KDACs use nicotinamide adenine dinucleotide (NAD) as a cofactor. Zinc-dependent KDACs fall into three main classes, including class I (KDACs 1, 2, 3, and 8), class II, further subdivided into class IIa (KDACs 4, 5, 7, and 9) and class IIb (KDAC 6 and 10), and class IV (KDAC 11).
Lysine deacetylases are an epigenetic drug targets of humans, and a broad range of small-molecule inhibitors for these have been reported. In recent years, lysine deacetylases have emerged as an important class of drug targets with the potential to treat psychiatric diseases, neurodegenerative diseases, and cancer. Notwithstanding, there remains a need for new treatment methods for other diseases such as those caused by parasites.